GLPB_SALSV
ID GLPB_SALSV Reviewed; 419 AA.
AC B4TPG8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G-3-P dehydrogenase subunit B {ECO:0000255|HAMAP-Rule:MF_00753};
DE Short=Anaerobic G3Pdhase B {ECO:0000255|HAMAP-Rule:MF_00753};
DE EC=1.1.5.3 {ECO:0000255|HAMAP-Rule:MF_00753};
GN Name=glpB {ECO:0000255|HAMAP-Rule:MF_00753}; OrderedLocusNames=SeSA_A2513;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses
CC fumarate or nitrate as electron acceptor. {ECO:0000255|HAMAP-
CC Rule:MF_00753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00753};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00753};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC GlpC. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC -!- SIMILARITY: Belongs to the anaerobic G-3-P dehydrogenase subunit B
CC family. {ECO:0000255|HAMAP-Rule:MF_00753}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001127; ACF91260.1; -; Genomic_DNA.
DR RefSeq; WP_000667152.1; NC_011094.1.
DR AlphaFoldDB; B4TPG8; -.
DR EnsemblBacteria; ACF91260; ACF91260; SeSA_A2513.
DR KEGG; sew:SeSA_A2513; -.
DR HOGENOM; CLU_047793_0_0_6; -.
DR OMA; CFGLENQ; -.
DR UniPathway; UPA00618; UER00673.
DR Proteomes; UP000001865; Chromosome.
DR GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00753; Glycerol3P_GlpB; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009158; G3P_DH_GlpB_su.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR03378; glycerol3P_GlpB; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..419
FT /note="Anaerobic glycerol-3-phosphate dehydrogenase subunit
FT B"
FT /id="PRO_1000133374"
SQ SEQUENCE 419 AA; 45724 MW; D2BF55EF1C6D73A9 CRC64;
MKFDTVIMGG GLAGLLCGLQ LQQHGLRCAI VTRGQSALHF SSGSLDLLSA LPDGQPVTDI
TAGLDALRRQ APEHPYSRLG AQKVLTLAQQ AQTLLNASGA QLYGDVQQAH QRVTPLGTLR
STWLSSPEVP VWPLSAQRIC VVGVSGLLDF QAHLAAASLR QRDLNVETAE IDLPELDVLR
DNPTEFRAVN IARLLDNEEK WPLLYDALSP IATNCDMIIM PACFGLANDT LWRWLNERLP
CALTLLPTLP PSVLGIRLHN QLQRQFVRQG GIWMPGDEVK KVTCRRGTVS EIWTRNHADI
PLRPRFAVLA SGSFFSSGLV AEREGIREPI LGLDVQQTAT RAEWYQQHFF DPQPWQQFGV
VTDDAFRPSL AGNTVENLYA IGSVLAGFDP IAEGCGGGVC AVSALQAAHH IAERAGEQQ